In vitro DNA-binding studies of cyclic AMP responsive element binding protein and CCAAT/enhancer binding protein beta

Basic region-leucine zipper (bZIP) proteins are an abundant class of eukaryotic transcription factors that bind to sequence-specific double-stranded DNS as homodimers or heterodimers to either activate or repress gene transcription. As a transcription factors bZIP proteins can be used as a targets for drug design to modulate gene transcription and ultimately control disease development.; The thesis project is focused on characterizing the stability of bZIP-DNA complexes. In particular, in vitro DNA binding of two bZIP transcriptional activators, CAMP-responsive element binding protein (CREB) and CCAAT/enhancer binding protein beta (C/EBPbeta), members of different bZIP protein families was investigated by using electrophoretic mobility shift assay (EMSA). Our experiments assessed the thermodynamic stability of homodimeric bZIP (C/EBP-C/EBP; CREB-CREB)-DNA complexes and the possibility of in vitro heterodimer (CREB-CIEBP) formation.